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Conserved domains on  [gi|194272148|ref|NP_001123543|]
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epsin-1 isoform a [Homo sapiens]

Protein Classification

ENTH domain-containing protein( domain architecture ID 13016662)

ENTH (Epsin N-Terminal Homology) domain-containing protein may be involved in clathrin-mediated endocytosis; similar to epsin that plays an important role as accessory proteins in clathrin-mediated endocytosis

CATH:  1.25.40.90
Gene Ontology:  GO:0030276|GO:0005543|GO:0006897|GO:1901981|GO:0072659
PubMed:  10567358|27466364|14657269|12742163|22748146|11911874|29774507
SCOP:  4001355

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ENTH_Epsin cd16990
Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an ...
 130-253 4.77e-98

Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an important role as accessory proteins in clathrin-mediated endocytosis. They are important factors in clathrin-coated vesicle (CCV) generation. They contribute to membrane deformation and play a key function as adaptor proteins, coupling various components of clathrin-mediated uptake. They also have an important role in selecting and recognizing cargo. Three isoforms have been identified in mammals, epsin-1 to -3, and these are conserved in vertebrates. Epsin-1 is highly enriched and represents the dominant isoform in the brain. It is required for proper synaptic vesicle retrieval and modulates the endocytic capacity of synaptic vesicles. Epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. The ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of CCVs. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


:

Pssm-ID: 340787  Cd Length: 124  Bit Score: 296.19  E-value: 4.77e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 130 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKE 209
Cdd:cd16990    1 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKALTLLEYLIKTGSERVAQQCKE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 194272148 210 NMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLRE 253
Cdd:cd16990   81 NIFAIQTLKDFQYIDRDGKDQGVNVREKAKQLVSLLKDDERLKN 124
PRK07764 super family cl35613
DNA polymerase III subunits gamma and tau; Validated
 351-524 2.47e-07

DNA polymerase III subunits gamma and tau; Validated


The actual alignment was detected with superfamily member PRK07764:

Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 54.22  E-value: 2.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 351 TAPAPAPTTDPWGGPAPMAAAVPTAAPTSDPWGGPPVPPAAdPWGGPAPTPASGDPWRPaaPAGPSVDPWGGTPAPAAGE 430
Cdd:PRK07764 652 HHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAA-PAGAAPAQPAPAPAATP--PAGQADDPAAQPPQAAQGA 728

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 431 GPTPdpwGSSDGGVPVSGPSASDPWTPAPAFSDPWGGSPAKPSTNGTTAAGGFDTEPDEFSDFDrlrtALPTSGSSAGEL 510
Cdd:PRK07764 729 SAPS---PAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDD----APSMDDEDRRDA 801

                        170
                 ....*....|....
gi 194272148 511 ELLAGEVPARSPGA 524
Cdd:PRK07764 802 EEVAMELLEEELGA 815
 
Name Accession Description Interval E-value
ENTH_Epsin cd16990
Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an ...
 130-253 4.77e-98

Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an important role as accessory proteins in clathrin-mediated endocytosis. They are important factors in clathrin-coated vesicle (CCV) generation. They contribute to membrane deformation and play a key function as adaptor proteins, coupling various components of clathrin-mediated uptake. They also have an important role in selecting and recognizing cargo. Three isoforms have been identified in mammals, epsin-1 to -3, and these are conserved in vertebrates. Epsin-1 is highly enriched and represents the dominant isoform in the brain. It is required for proper synaptic vesicle retrieval and modulates the endocytic capacity of synaptic vesicles. Epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. The ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of CCVs. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


Pssm-ID: 340787  Cd Length: 124  Bit Score: 296.19  E-value: 4.77e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 130 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKE 209
Cdd:cd16990    1 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKALTLLEYLIKTGSERVAQQCKE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 194272148 210 NMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLRE 253
Cdd:cd16990   81 NIFAIQTLKDFQYIDRDGKDQGVNVREKAKQLVSLLKDDERLKN 124
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 128-251 3.01e-72

ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in endocytosis and cytoskeletal machinery. The function of the ENTH domain is unknown.


Pssm-ID: 426255  Cd Length: 124  Bit Score: 228.98  E-value: 3.01e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148  128 YSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQC 207
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKRLNDKGKNWRHIYKALTLLEYLLKNGSERVVDDL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 194272148  208 KENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRL 251
Cdd:pfam01417  81 RENIYIIRTLTDFHYIDENGKDQGINVRKKAKEILNLLEDDELL 124
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
129-255 4.36e-52

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 175.51  E-value: 4.36e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148   129 SEAEIKVREATSNDPWGPSSSLMSEIADLTYNV-VAFSEIMSMIWKRLNDHGkNWRHVYKAMTLMEYLIKTGSERVSQQC 207
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEkSSFAEIMAVLWRRLNDTK-NWRVVYKALILLHYLLRNGSPRVILEA 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 194272148   208 KENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREER 255
Cdd:smart00273  80 LRNRNRILNLSDFQDIDSRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 351-524 2.47e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 54.22  E-value: 2.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 351 TAPAPAPTTDPWGGPAPMAAAVPTAAPTSDPWGGPPVPPAAdPWGGPAPTPASGDPWRPaaPAGPSVDPWGGTPAPAAGE 430
Cdd:PRK07764 652 HHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAA-PAGAAPAQPAPAPAATP--PAGQADDPAAQPPQAAQGA 728

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 431 GPTPdpwGSSDGGVPVSGPSASDPWTPAPAFSDPWGGSPAKPSTNGTTAAGGFDTEPDEFSDFDrlrtALPTSGSSAGEL 510
Cdd:PRK07764 729 SAPS---PAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDD----APSMDDEDRRDA 801

                        170
                 ....*....|....
gi 194272148 511 ELLAGEVPARSPGA 524
Cdd:PRK07764 802 EEVAMELLEEELGA 815
MSCRAMM_ClfB NF033845
MSCRAMM family adhesin clumping factor ClfB; Clumping factor B is an MSCRAMM (Microbial ...
 380-494 1.77e-04

MSCRAMM family adhesin clumping factor ClfB; Clumping factor B is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468203 [Multi-domain]  Cd Length: 871  Bit Score: 44.94  E-value: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 380 DPWGGPPVPPAADPWGGPAPTPasgdpwrpaapaGPSVDPwggTPAPAAGEGPTPDPWGSSDGGVPVSGPSASDPWTPAP 459
Cdd:NF033845 545 DPTPGPPVDPEPSPEPEPEPTP------------DPEPSP---DPDPEPSPDPDPDSDSDSDSGSDSDSGSDSDSDSDSD 609

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 194272148 460 AFSDPWGGSPAKPSTNGTTAAggfDTEPDEFSDFD 494
Cdd:NF033845 610 SDSDSDSDSDSDSDSDSDSDS---DSDSDSDSDSD 641
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
 386-483 2.39e-03

Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix.


Pssm-ID: 429334  Cd Length: 301  Bit Score: 40.68  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148  386 PVPPAADPWGGPAPTPASGDPWRPAAPAGPSVDPwGGTPAPAAGEGPTPDPWGSSDGGVPvsgPSASDPWTPAPAFSDPW 465
Cdd:pfam07174  34 PAVAHADPEPAPPPPSTATAPPAPPPPPPAPAAP-APPPPPAAPNAPNAPPPPADPNAPP---PPPADPNAPPPPAVDPN 109

                          90
                  ....*....|....*...
gi 194272148  466 GGSPAKPstngTTAAGGF 483
Cdd:pfam07174 110 APEPGRI----DNAVGGF 123
 
Name Accession Description Interval E-value
ENTH_Epsin cd16990
Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an ...
 130-253 4.77e-98

Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an important role as accessory proteins in clathrin-mediated endocytosis. They are important factors in clathrin-coated vesicle (CCV) generation. They contribute to membrane deformation and play a key function as adaptor proteins, coupling various components of clathrin-mediated uptake. They also have an important role in selecting and recognizing cargo. Three isoforms have been identified in mammals, epsin-1 to -3, and these are conserved in vertebrates. Epsin-1 is highly enriched and represents the dominant isoform in the brain. It is required for proper synaptic vesicle retrieval and modulates the endocytic capacity of synaptic vesicles. Epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. The ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of CCVs. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


Pssm-ID: 340787  Cd Length: 124  Bit Score: 296.19  E-value: 4.77e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 130 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKE 209
Cdd:cd16990    1 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKALTLLEYLIKTGSERVAQQCKE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 194272148 210 NMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLRE 253
Cdd:cd16990   81 NIFAIQTLKDFQYIDRDGKDQGVNVREKAKQLVSLLKDDERLKN 124
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 128-251 3.01e-72

ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in endocytosis and cytoskeletal machinery. The function of the ENTH domain is unknown.


Pssm-ID: 426255  Cd Length: 124  Bit Score: 228.98  E-value: 3.01e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148  128 YSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQC 207
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKRLNDKGKNWRHIYKALTLLEYLLKNGSERVVDDL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 194272148  208 KENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRL 251
Cdd:pfam01417  81 RENIYIIRTLTDFHYIDENGKDQGINVRKKAKEILNLLEDDELL 124
ENTH_Ent1_Ent2 cd16991
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent1, Ent2, and similar proteins; This ...
 128-255 1.20e-69

Epsin N-Terminal Homology (ENTH) domain of Yeast Ent1, Ent2, and similar proteins; This subfamily is composed of the two orthologs of epsin in Saccharomyces cerevisiae, Epsin-1 (Ent1 or Ent1p) and Epsin-2 (Ent2 or Ent2p), and similar proteins. Yeast single epsin knockouts, either Ent1 and Ent2, are viable while the double knockout is not. Yeast epsins are required for endocytosis and localization of actin. Ent2 also plays a signaling role during cell division. The ENTH domain of Ent2 interacts with the septin organizing, Cdc42 GTPase activating protein, Bem3, leading to increased cytokinesis failure when overexpressed. Yeast epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


Pssm-ID: 340788  Cd Length: 132  Bit Score: 222.53  E-value: 1.20e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 128 YSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQC 207
Cdd:cd16991    2 YSSTQVKVRNATSNDPWGPSGDEMAEIAELTYDQHDFVEIMDMLDKRLNDKGKNWRHVAKALTVLDYLLHFGSENVVLWA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 194272148 208 KENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREER 255
Cdd:cd16991   82 KENIYIIKTLREFQYIDDEGKDQGQNVRVKAKELTSLLLDDERLREER 129
ENTH cd03571
Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is ...
 131-247 1.08e-64

Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, contributing to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


Pssm-ID: 340772  Cd Length: 117  Bit Score: 208.91  E-value: 1.08e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 131 AEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKEN 210
Cdd:cd03571    1 LELLVREATSNEPWGPTGSQLAEIAQATFDYDDYQRIMKVLWKRLNDKGKNWRHVYKALTLLEYLLKNGSERVVDEFRDN 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 194272148 211 MYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRD 247
Cdd:cd03571   81 LYLIRTLQDFQYVDENGDDQGINVREKAKQIVALLED 117
ENTH_EpsinR cd16989
Epsin N-Terminal Homology (ENTH) domain of Epsin-related protein; Epsin-related protein ...
 131-258 1.18e-59

Epsin N-Terminal Homology (ENTH) domain of Epsin-related protein; Epsin-related protein (EpsinR) is also called clathrin interactor 1 (Clint), enthoprotin, or epsin-4. It is a clathrin-coated vesicle (CCV) protein that binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), clathrin, and the gamma appendage domain of the adaptor protein complex 1 (AP1). It contains an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. The ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. The ENTH domain of human epsinR binds directly to the helical bundle domain of the mouse SNARE Vti1b; soluble NSF attachment protein receptors (SNAREs) are type II transmembrane proteins that have critical roles in providing the specificity and energy for transport-vesicle fusion. Specific ENTH domains may also function as protein cargo selection/recognition modules. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


Pssm-ID: 340786  Cd Length: 130  Bit Score: 195.97  E-value: 1.18e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 131 AEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKR-LNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKE 209
Cdd:cd16989    1 IESKVREATNDDPWGPTGQLMQEIARYTFTYEQFPEVMNMLWKRmLKDNKKNWRRVYKSLLLLDYLLKNGSERVVTSARE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 194272148 210 NMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREERAHA 258
Cdd:cd16989   81 HIYDLRSLENYHFIDEKGKDQGINVRQKVKEIIELLQDDERLREERKKA 129
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
129-255 4.36e-52

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 175.51  E-value: 4.36e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148   129 SEAEIKVREATSNDPWGPSSSLMSEIADLTYNV-VAFSEIMSMIWKRLNDHGkNWRHVYKAMTLMEYLIKTGSERVSQQC 207
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEkSSFAEIMAVLWRRLNDTK-NWRVVYKALILLHYLLRNGSPRVILEA 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 194272148   208 KENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREER 255
Cdd:smart00273  80 LRNRNRILNLSDFQDIDSRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
ENTH_Ent3 cd16992
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent3 and similar proteins; This subfamily is ...
 132-250 1.67e-45

Epsin N-Terminal Homology (ENTH) domain of Yeast Ent3 and similar proteins; This subfamily is composed of one of two epsinR orthologs present in Saccharomyces cerevisiae, Epsin-3 (Ent3 or Ent3p), and similar proteins. Ent3 is an adaptor proteins at the Trans-Golgi Network (TGN); it cooperates with yeast SNARE Vti1p to regulate transport from the TGN to the prevacuolar endosome. Ent3 facilitates the interaction between Gga2p with both the endosomal syntaxin Pep12p and clathrin in the GGA-dependent transport to the late endosome. Yeast epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. Similar to mammalian epsinR, The ENTH domain of Ent3 binds to the yeast SNARE Vti1p; soluble NSF attachment protein receptors (SNAREs) are type II transmembrane proteins that have critical roles in providing the specificity and energy for transport-vesicle fusion. Specific ENTH domains may also function as protein cargo selection/recognition modules. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


Pssm-ID: 340789  Cd Length: 121  Bit Score: 157.61  E-value: 1.67e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 132 EIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLND-HGKNWRHVYKAMTLMEYLIKTGSERVSQQCKEN 210
Cdd:cd16992    2 ESKVREATNNDPWGASSTLMQEIAQGTYNYQQFNEIMPMIYKRFTEkAGSEWRQIYKALQLLEYLIKNGSERVVDDARGH 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 194272148 211 MYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDR 250
Cdd:cd16992   82 LTLIKMLRSFHYIDDKGKDQGINVRNRAKELIELLSDDEK 121
VHS_ENTH_ANTH cd00197
VHS, ENTH and ANTH domain superfamily; This superfamily is composed of proteins containing a ...
 131-247 1.47e-40

VHS, ENTH and ANTH domain superfamily; This superfamily is composed of proteins containing a VHS, CID, ENTH, or ANTH domain. The VHS domain is present in Vps27 (Vacuolar Protein Sorting), Hrs (Hepatocyte growth factor-regulated tyrosine kinase substrate) and STAM (Signal Transducing Adaptor Molecule). It is located at the N-termini of proteins involved in intracellular membrane trafficking. The CTD-Interacting Domain (CID) is present in several RNA-processing factors and binds tightly to the carboxy-terminal domain (CTD) of RNA polymerase II (RNAP II or Pol II). The epsin N-terminal homology (ENTH) domain is an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. A set of proteins previously designated as harboring an ENTH domain in fact contains a highly similar, yet unique module referred to as an AP180 N-Terminal Homology (ANTH) domain. VHS, ENTH, and ANTH domains are structurally similar and are composed of a superhelix of eight alpha helices. ENTH and ANTH (E/ANTH) domains bind both inositol phospholipids and proteins and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. E/ANTH domain-bearing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


Pssm-ID: 340764  Cd Length: 115  Bit Score: 143.72  E-value: 1.47e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 131 AEIKVREATSNDPWGPSSSLMSEIADLTYN-VVAFSEIMSMIWKRLNDHgkNWRHVYKAMTLMEYLIKTGSERVSQQCKE 209
Cdd:cd00197    1 FEKTVEKATSNENMGPDWPLIMEICDLINEtNVGPKEAVDAIKKRINNK--NPHVVLKALTLLEYCVKNCGERFHQEVAS 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 194272148 210 NMYAVQTLKdFQYVDRDGKDQGVNVREKAKQLVALLRD 247
Cdd:cd00197   79 NDFAVELLK-FDKSGLLGDDVSTNVREKAIELVQLWAS 115
ENTH_Ent4 cd16994
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent4 and similar proteins; Yeast Epsin-4 ...
 131-249 1.53e-21

Epsin N-Terminal Homology (ENTH) domain of Yeast Ent4 and similar proteins; Yeast Epsin-4 (Ent4 or Ent4p) has been reported to be involved in the Trans-Golgi Network (TGN)-to-vacuole sorting of Arn1p, a transporter for the uptake of ferrichrome, an important nutritional source of iron. Yeast epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


Pssm-ID: 340791  Cd Length: 126  Bit Score: 90.43  E-value: 1.53e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 131 AEIKVREAT-SNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHG-----KNWRHVYKAMTLMEYLIKTGSERVS 204
Cdd:cd16994    1 TELKVKQATdDNETSGATGTLMNEISVLTYSPKTLKEITQVLKKRLSGNSkksshKNCVHILKTLTLISYLINNGSNEFI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 194272148 205 QQCKENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDED 249
Cdd:cd16994   81 AWLRSNLYLIERLKDFEVQDNRDLPMANQIRSLSQDICELINDDE 125
ENTH_Ent5 cd16993
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent5 and similar proteins; This subfamily is ...
 132-256 1.12e-08

Epsin N-Terminal Homology (ENTH) domain of Yeast Ent5 and similar proteins; This subfamily is composed of one of two epsinR orthologs present in Saccharomyces cerevisiae, Epsin-5 (Ent5 or Ent5p), and similar proteins. Ent5 is required, together with Ent3 and Vps27p for ubiquitin-dependent protein sorting into the multivesicular body. It is also required for protein transport from the Trans-Golgi Network (TGN) to the vacuole. Yeast epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


Pssm-ID: 340790  Cd Length: 158  Bit Score: 54.78  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 132 EIKVREATSNDPWGPSSSLMSEIADLTYNVVAFsEIMSMIWKRLNDH-------------------GKNWRHVYKAMTLM 192
Cdd:cd16993    2 QIDIRRATNTDAWGPTPKHLAKVLRNRYQVPLY-LMTEYTLKRLVDHiatrpknlyekarkdyvnyGSEWRVVLKCLIVI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194272148 193 EYLIKTGS--ERVSQ--QCKENMYAVQTLKDFQY---VDRDGKDQ--GVNVREKAKQLVALLRDEDRLREERA 256
Cdd:cd16993   81 EFLLLNVDtgDELNQvlSCLLNHKHIFTREIAQYkvkFSNDGKMEihERGIQKKCELILQLIEDSDFLRQERA 153
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 351-524 2.47e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 54.22  E-value: 2.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 351 TAPAPAPTTDPWGGPAPMAAAVPTAAPTSDPWGGPPVPPAAdPWGGPAPTPASGDPWRPaaPAGPSVDPWGGTPAPAAGE 430
Cdd:PRK07764 652 HHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAA-PAGAAPAQPAPAPAATP--PAGQADDPAAQPPQAAQGA 728

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 431 GPTPdpwGSSDGGVPVSGPSASDPWTPAPAFSDPWGGSPAKPSTNGTTAAGGFDTEPDEFSDFDrlrtALPTSGSSAGEL 510
Cdd:PRK07764 729 SAPS---PAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDD----APSMDDEDRRDA 801

                        170
                 ....*....|....
gi 194272148 511 ELLAGEVPARSPGA 524
Cdd:PRK07764 802 EEVAMELLEEELGA 815
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 351-540 3.90e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 53.45  E-value: 3.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 351 TAPAPAPTTDPWGGPAPMAAAVPTAAPTSDPWGGPPVP--------PAADPWGGPAPTPASGDPWRPAAPAGPSVDPWG- 421
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPapagaaaaPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGw 669

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 422 ----GTPAPAAGEGPTPDPWGSSDGGVPVSGPSASDPWTPAPAFSDPWGGSPAKPSTNGTTAAGGFDTEPDEFSDFDRLR 497
Cdd:PRK07764 670 pakaGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPP 749

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 194272148 498 TALPTSGSSAGELELLAGEVPARSPGAFDMSGVRGSLAEAVGS 540
Cdd:PRK07764 750 DPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPS 792
PHA03247 PHA03247
large tegument protein UL36; Provisional
 353-612 2.37e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 2.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148  353 PAPAPTTDPWGGPAPMAAAVPTAAPTSDPWGGPPVPPAadPWGGPAPTPASGDPWRPAAPAGPSvdpwggTPAPAAGEGP 432
Cdd:PHA03247 2706 PTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPA--VPAGPATPGGPARPARPPTTAGPP------APAPPAAPAA 2777

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148  433 TPDPWGSSDGGVP--VSGPSASDPWTPA--------PAFSDPWGGSPAKPSTNGTTAAGGFDTEPDEFsdfdrLRTALPT 502
Cdd:PHA03247 2778 GPPRRLTRPAVASlsESRESLPSPWDPAdppaavlaPAAALPPAASPAGPLPPPTSAQPTAPPPPPGP-----PPPSLPL 2852

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148  503 SGSSAGelellAGEVPARSPGafdmsgvRGSLAEAVGSPPPAATPTPTPPTRKTPESFLGPNaalvdlDSLVSRPGPTPP 582
Cdd:PHA03247 2853 GGSVAP-----GGDVRRRPPS-------RSPAAKPAAPARPPVRRLARPAVSRSTESFALPP------DQPERPPQPQAP 2914

                         250       260       270
                  ....*....|....*....|....*....|
gi 194272148  583 GAKASNPFLPGGGPATGPSVTNPFQPAPPA 612
Cdd:PHA03247 2915 PPPQPQPQPPPPPQPQPPPPPPPRPQPPLA 2944
PHA03247 PHA03247
large tegument protein UL36; Provisional
 354-613 3.36e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 3.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148  354 APAPTTDPWGGPAPMAAAVPTAAPTS-----DPWGGPPVPPAADPWGGPAPTPAS---GDPWRPAAPAGPSVDPWGGTPA 425
Cdd:PHA03247 2491 AAGAAPDPGGGGPPDPDAPPAPSRLApailpDEPVGEPVHPRMLTWIRGLEELASddaGDPPPPLPPAAPPAAPDRSVPP 2570

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148  426 PAAGEGPtPDPWGSSDGGVPVSGPSASDPWTPAPAFSDPWGGSPAKPSTNGTTAAggfdtEPDEFSDFDRlrtalptsGS 505
Cdd:PHA03247 2571 PRPAPRP-SEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAP-----DPPPPSPSPA--------AN 2636

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148  506 SAGELELLAGEVPARSPGAFDMSGVRGSLAEAVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGAK 585
Cdd:PHA03247 2637 EPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALV 2716

                         250       260
                  ....*....|....*....|....*...
gi 194272148  586 ASNPFLPGGGPATGPSVTNPFQPAPPAT 613
Cdd:PHA03247 2717 SATPLPPGPAAARQASPALPAAPAPPAV 2744
VHS cd03561
VHS (Vps27/Hrs/STAM) domain family; The VHS domain is present in Vps27 (Vacuolar Protein ...
 135-242 1.42e-05

VHS (Vps27/Hrs/STAM) domain family; The VHS domain is present in Vps27 (Vacuolar Protein Sorting), Hrs (Hepatocyte growth factor-regulated tyrosine kinase substrate) and STAM (Signal Transducing Adaptor Molecule). It has a superhelical structure similar to that of the ARM (Armadillo) repeats and is present at the N-termini of proteins involved in intracellular membrane trafficking. There are four general groups of VHS domain containing proteins based on their association with other domains. The first group consists of proteins of the STAM/EAST/Hbp family, which has the domain composition of VHS-SH3-ITAM. The second consists of proteins with a FYVE domain C-terminal to VHS. The third consists of GGA proteins with a domain composition of VHS-GAT (GGA and TOM)-GAE (Gamma-Adaptin Ear) domain. The fourth consists of proteins with a VHS domain alone or with domains other than those mentioned above. In GGA proteins, VHS domains are involved in cargo recognition in trans-Golgi, thereby having a general membrane targeting/cargo recognition role in vesicular trafficking.


Pssm-ID: 340765  Cd Length: 131  Bit Score: 44.95  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 135 VREATSNDPWGPSSSLMSEIADLtYNVVAFS--EIMSMIWKRLNDhgKNWRHVYKAMTLMEYLIKTGSERVSQQckenmy 212
Cdd:cd03561    5 VEKATSESLTEPDWALNLEICDL-VNSDPAQakDAVRALRKRLQS--KNPKVQLLALTLLETLVKNCGAPFHSE------ 75

                         90       100       110
                 ....*....|....*....|....*....|..
gi 194272148 213 aVQTLKDFQYVDR--DGKDQGVNVREKAKQLV 242
Cdd:cd03561   76 -VASRDFLQELVKlvKKKKTSPEVREKALALI 106
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
347-520 5.12e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 46.41  E-value: 5.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 347 ADVFTAPAPAPTTDPWGGPAPMAAAVPTAAPTSDPWGGPPVPPAADPWGGPAPTPASGDPwRPAAPAGPSVDPWGGTP-- 424
Cdd:PRK12323 404 AAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAAR-PAAAGPRPVAAAAAAAPar 482

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 425 -APAAGEGPTPD---PWGSSDGGVPVSGPSASDP--------WTPAPAFSDPWGGSPAKPSTNGTTAAGGFDTEPDEFSD 492
Cdd:PRK12323 483 aAPAAAPAPADDdppPWEELPPEFASPAPAQPDAapagwvaeSIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVA 562

                        170       180
                 ....*....|....*....|....*....
gi 194272148 493 FDRLRTALP-TSGSSAGELELLAGEVPAR 520
Cdd:PRK12323 563 PRPPRASASgLPDMFDGDWPALAARLPVR 591
MSCRAMM_ClfB NF033845
MSCRAMM family adhesin clumping factor ClfB; Clumping factor B is an MSCRAMM (Microbial ...
 380-494 1.77e-04

MSCRAMM family adhesin clumping factor ClfB; Clumping factor B is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468203 [Multi-domain]  Cd Length: 871  Bit Score: 44.94  E-value: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 380 DPWGGPPVPPAADPWGGPAPTPasgdpwrpaapaGPSVDPwggTPAPAAGEGPTPDPWGSSDGGVPVSGPSASDPWTPAP 459
Cdd:NF033845 545 DPTPGPPVDPEPSPEPEPEPTP------------DPEPSP---DPDPEPSPDPDPDSDSDSDSGSDSDSGSDSDSDSDSD 609

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 194272148 460 AFSDPWGGSPAKPSTNGTTAAggfDTEPDEFSDFD 494
Cdd:NF033845 610 SDSDSDSDSDSDSDSDSDSDS---DSDSDSDSDSD 641
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 352-540 3.62e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.01  E-value: 3.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148  352 APAPAPTTDPWGGPAPMAAAVPTAAPTSDPWGGPPVPPAADPWGGPAPTPASGDPwrPAAPAGPSVDPWGGTPAPAAGEG 431
Cdd:PHA03307   81 ANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLS--EMLRPVGSPGPPPAASPPAAGAS 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148  432 PTPDPWGSSDGG--------VPVSGPSASDPWTPAPAFSDPWGGSPAKPSTNGTTAAGGFDTEPDEFSDFDRLRTALPTS 503
Cdd:PHA03307  159 PAAVASDAASSRqaalplssPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSD 238

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 194272148  504 GSSAGELELLAG---EVPARSPGAFDMSGVRGSLAEAVGS 540
Cdd:PHA03307  239 SSSSESSGCGWGpenECPLPRPAPITLPTRIWEASGWNGP 278
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
351-524 8.09e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.56  E-value: 8.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 351 TAPAPAPTTDPWGGPAPMAAAVPTAAPTSDPwggPPVPPAADPWGGPAPTPASGDPWRPAAPAGPSVDPWGGTPAPAAGE 430
Cdd:PRK12323 393 AAAAPAPAAPPAAPAAAPAAAAAARAVAAAP---ARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGP 469

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 431 GPTPD-----PWGSSDGGVPVSGPSASDPWTPAPAFSDPWGGSPAKPSTNGTTAAGGFDTEPDEFSDFDRLRTALPTSGS 505
Cdd:PRK12323 470 RPVAAaaaaaPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAP 549

                        170
                 ....*....|....*....
gi 194272148 506 SAGELELLAGEVPARSPGA 524
Cdd:PRK12323 550 APRAAAATEPVVAPRPPRA 568
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 352-465 8.76e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.67  E-value: 8.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 352 APAPAPTTDPWGGPAPMAAAVPTAAPTSDPWGGPPVPPAADPWGGPAPTPASGDPWRPAAPAGPSVDPWGGTPAPAAGEG 431
Cdd:PRK07764 402 AAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPA 481

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 194272148 432 PTPDPWGSSDGGVPV-SGPSASDPWTPAPAFSDPW 465
Cdd:PRK07764 482 PAPPAAPAPAAAPAApAAPAAPAGADDAATLRERW 516
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 381-539 1.48e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 381 PWGGPPVPPAADPWGGPAPTPASGDPwrPAAPAGPSVDPwgGTPAPAAGEGPTPDPwgssdggVPVSGPSASDPWTPAPA 460
Cdd:PRK07764 386 GVAGGAGAPAAAAPSAAAAAPAAAPA--PAAAAPAAAAA--PAPAAAPQPAPAPAP-------APAPPSPAGNAPAGGAP 454

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194272148 461 fSDPWGGSPAKPSTNGTTAAGGFDTEPdefsdfdrlrtALPTSGSSAGELELLAGEVPARSPGAFDMSGVRGSLAEAVG 539
Cdd:PRK07764 455 -SPPPAAAPSAQPAPAPAAAPEPTAAP-----------APAPPAAPAPAAAPAAPAAPAAPAGADDAATLRERWPEILA 521
PHA03247 PHA03247
large tegument protein UL36; Provisional
 352-610 1.90e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148  352 APAPAPTTDPWGGPAPMAAAVPTAAPTSDPWGGPPVPPAADPWGGPAPTPASGdPWRPAAP---------AGPSVDPWGG 422
Cdd:PHA03247 2630 SPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQR-PRRRAARptvgsltslADPPPPPPTP 2708

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148  423 TPAPAAGEGPTPDPWGSSDGGVPVSGPSAsDPWTPAPAFSDPWGGSPAKPSTNGTTAAGGFDTEP-DEFSDFDRLRTALP 501
Cdd:PHA03247 2709 EPAPHALVSATPLPPGPAAARQASPALPA-APAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPaAPAAGPPRRLTRPA 2787

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148  502 TSGSSAGELELLAGEVPARSPGAFD--MSGVRGSLAEAVGSPP-PAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPG 578
Cdd:PHA03247 2788 VASLSESRESLPSPWDPADPPAAVLapAAALPPAASPAGPLPPpTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPP 2867

                         250       260       270
                  ....*....|....*....|....*....|..
gi 194272148  579 PTPPGAKASNPFLPGGGPATGPSVTNPFQPAP 610
Cdd:PHA03247 2868 SRSPAAKPAAPARPPVRRLARPAVSRSTESFA 2899
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
 386-483 2.39e-03

Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix.


Pssm-ID: 429334  Cd Length: 301  Bit Score: 40.68  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148  386 PVPPAADPWGGPAPTPASGDPWRPAAPAGPSVDPwGGTPAPAAGEGPTPDPWGSSDGGVPvsgPSASDPWTPAPAFSDPW 465
Cdd:pfam07174  34 PAVAHADPEPAPPPPSTATAPPAPPPPPPAPAAP-APPPPPAAPNAPNAPPPPADPNAPP---PPPADPNAPPPPAVDPN 109

                          90
                  ....*....|....*...
gi 194272148  466 GGSPAKPstngTTAAGGF 483
Cdd:pfam07174 110 APEPGRI----DNAVGGF 123
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
351-489 2.85e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.01  E-value: 2.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 351 TAPAPAPTTDPWGGPAPMAAAVPTAAPTSDPWGGPPVPPAADPwggPAPTPASGDPWRPAAPAGPSVDPWGGTPAPAAGE 430
Cdd:PRK12323 372 AGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAA---AARAVAAAPARRSPAPEALAAARQASARGPGGAP 448

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 194272148 431 GPTPDPwgssdggVPVSGPSASDPWTPAPAFSDPWGGSPAKPSTNGTTAAGGFDTEPDE 489
Cdd:PRK12323 449 APAPAP-------AAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWE 500
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 351-613 3.02e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.92  E-value: 3.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148  351 TAPAPAPTTDPWGGPAPMAAAVPTAAPTSDPWGGPPVPPAADPWGGPAPTPASGDPWRPAAPAGPSVDPWGGTPAPaage 430
Cdd:PHA03307  113 SPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSS---- 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148  431 gPTPDPWGSSDGGVPVSGPSASDPWTPAPAFSDPWGGSPAKPSTNGTTAAGGFDTEPDEFSDFDRLRTALPTSGSSAGEL 510
Cdd:PHA03307  189 -PPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPT 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148  511 ELLAGEVPARSPGAFDMSGVRGSLAEAVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGAKASNPF 590
Cdd:PHA03307  268 RIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSP 347

                         250       260
                  ....*....|....*....|...
gi 194272148  591 LPGGGPATGPSvtnPFQPAPPAT 613
Cdd:PHA03307  348 SRSPSPSRPPP---PADPSSPRK 367
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 348-451 3.24e-03

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 40.64  E-value: 3.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148  348 DVFTAPAPAPTTDPwggpapmaaAVPTAAPTSDPWGGPPVPPAADPWGGPAPTPASGDPWRPAAPAGPSVDPWGGTPAPA 427
Cdd:PRK12270   31 EFFADYGPGSTAAP---------TAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPA 101

                          90       100
                  ....*....|....*....|....
gi 194272148  428 AGEGPTPDPWGSSDGGVPVSGPSA 451
Cdd:PRK12270  102 AAAAAAPAAAAVEDEVTPLRGAAA 125
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
381-488 7.61e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 39.45  E-value: 7.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 381 PWGGPPVPPAADPWGGPAPTPASGDPWRPAAPAGPSVDPWGGTPAPAAGEGPTPDPwGSSDGGVPVSGPSASDPWTPAPA 460
Cdd:PRK07003 381 PAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATA-DRGDDAADGDAPVPAKANARASA 459

                         90       100
                 ....*....|....*....|....*...
gi 194272148 461 FSDPWGGSPAKPSTNGTTAAGGFDTEPD 488
Cdd:PRK07003 460 DSRCDERDAQPPADSGSASAPASDAPPD 487
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 386-613 7.74e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.58  E-value: 7.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 386 PVPPAADPWGGPAPTPaSGDPWRPAAPAGPSVDPWGGTPAPAAGEGPTPDPWGSSDGGVPVSGPSASDPWTPAPAFS-DP 464
Cdd:PRK07764 590 PAPGAAGGEGPPAPAS-SGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGgDG 668

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 465 WGGSPAKPSTNGTTAAggfdtepdefsdfdrlrtalPTSGSSAGelellAGEVPARSPGAFDMSGVRGSLAEAVGSPPPA 544
Cdd:PRK07764 669 WPAKAGGAAPAAPPPA--------------------PAPAAPAA-----PAGAAPAQPAPAPAATPPAGQADDPAAQPPQ 723

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194272148 545 ATPTPTPPTRKTPESflGPNAALVDLDSLVSRPGPTPPGAKASNPFLPGGGPATGPSVTNPFQPAPPAT 613
Cdd:PRK07764 724 AAQGASAPSPAADDP--VPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDA 790
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 363-481 7.94e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.58  E-value: 7.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 363 GGPAPMAAAVPTAAPTSdpwgGPPVPPAADPwGGPAPTPASGDPWRPAAPAGPsvdpwggTPAPAAGEGPTPDPWGSSDG 442
Cdd:PRK07764 384 RLGVAGGAGAPAAAAPS----AAAAAPAAAP-APAAAAPAAAAAPAPAAAPQP-------APAPAPAPAPPSPAGNAPAG 451

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 194272148 443 GVPVS--GPSASDPWTPAPAFSDPWGGSPAKPSTNGTTAAG 481
Cdd:PRK07764 452 GAPSPppAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAA 492
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 349-460 9.58e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.20  E-value: 9.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194272148 349 VFTAPAPAPTTDPWGGPAPMAAAVPTAAPTSDPWGGPPVPPAA-DPWGGPAPTPASGDPWRPAAPAGPSVDPWGGTPA-- 425
Cdd:PRK07764 386 GVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAApQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSaq 465

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 194272148 426 PAAGEGPTPDPWGSSDGGVPVSGPSASDPWTPAPA 460
Cdd:PRK07764 466 PAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAP 500
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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